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Quantitative label-free phosphoproteomics of six different life stages of the late blight pathogen Phytophthora infestans reveals abundant phosphorylation of members of the CRN effector family

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Resjö, Svante ; Ali, Ashfaq ; Meijer, Harold J G ; Seidl, Michael F ; Snel, Berend ; Sandin, Marianne ; Levander, Fredrik ; Govers, Francine ; Andreasson, Erik. / Quantitative label-free phosphoproteomics of six different life stages of the late blight pathogen Phytophthora infestans reveals abundant phosphorylation of members of the CRN effector family. In: Journal of Proteome Research. 2014 ; Vol. 13, No. 4. pp. 1848-59.

Bibtex

@article{80439513804a4885bcc2d3566636ee58,
title = "Quantitative label-free phosphoproteomics of six different life stages of the late blight pathogen Phytophthora infestans reveals abundant phosphorylation of members of the CRN effector family",
abstract = "The oomycete Phytophthora infestans is the causal agent of late blight in potato and tomato. Since the underlying processes that govern pathogenicity and development in P. infestans are largely unknown, we have performed a large-scale phosphoproteomics study of six different P. infestans life stages. We have obtained quantitative data for 2922 phosphopeptides and compared their abundance. Life-stage-specific phosphopeptides include ATP-binding cassette transporters and a kinase that only occurs in appressoria. In an extended data set, we identified 2179 phosphorylation sites and deduced 22 phosphomotifs. Several of the phosphomotifs matched consensus sequences of kinases that occur in P. infestans but not Arabidopsis. In addition, we detected tyrosine phosphopeptides that are potential targets of kinases resembling mammalian tyrosine kinases. Among the phosphorylated proteins are members of the RXLR and Crinkler effector families. The latter are phosphorylated in several life stages and at multiple positions, in sites that are conserved between different members of the Crinkler family. This indicates that proteins in the Crinkler family have functions beyond their putative role as (necrosis-inducing) effectors. This phosphoproteomics data will be instrumental for studies on oomycetes and host-oomycete interactions. The data sets have been deposited to ProteomeXchange (identifier PXD000433).",
keywords = "Amino Acid Motifs, Amino Acid Sequence, Life Cycle Stages, Molecular Sequence Data, Phosphopeptides, Phosphoproteins, Phosphorylation, Phytophthora infestans, Protein-Serine-Threonine Kinases, Proteomics, Tissue Culture Techniques, Journal Article, Research Support, Non-U.S. Gov't",
author = "Svante Resj{\"o} and Ashfaq Ali and Meijer, {Harold J G} and Seidl, {Michael F} and Berend Snel and Marianne Sandin and Fredrik Levander and Francine Govers and Erik Andreasson",
year = "2014",
month = "4",
day = "4",
doi = "10.1021/pr4009095",
language = "English",
volume = "13",
pages = "1848--59",
journal = "Journal of Proteome Research",
issn = "1535-3893",
publisher = "American Chemical Society",
number = "4",

}

RIS

TY - JOUR

T1 - Quantitative label-free phosphoproteomics of six different life stages of the late blight pathogen Phytophthora infestans reveals abundant phosphorylation of members of the CRN effector family

AU - Resjö, Svante

AU - Ali, Ashfaq

AU - Meijer, Harold J G

AU - Seidl, Michael F

AU - Snel, Berend

AU - Sandin, Marianne

AU - Levander, Fredrik

AU - Govers, Francine

AU - Andreasson, Erik

PY - 2014/4/4

Y1 - 2014/4/4

N2 - The oomycete Phytophthora infestans is the causal agent of late blight in potato and tomato. Since the underlying processes that govern pathogenicity and development in P. infestans are largely unknown, we have performed a large-scale phosphoproteomics study of six different P. infestans life stages. We have obtained quantitative data for 2922 phosphopeptides and compared their abundance. Life-stage-specific phosphopeptides include ATP-binding cassette transporters and a kinase that only occurs in appressoria. In an extended data set, we identified 2179 phosphorylation sites and deduced 22 phosphomotifs. Several of the phosphomotifs matched consensus sequences of kinases that occur in P. infestans but not Arabidopsis. In addition, we detected tyrosine phosphopeptides that are potential targets of kinases resembling mammalian tyrosine kinases. Among the phosphorylated proteins are members of the RXLR and Crinkler effector families. The latter are phosphorylated in several life stages and at multiple positions, in sites that are conserved between different members of the Crinkler family. This indicates that proteins in the Crinkler family have functions beyond their putative role as (necrosis-inducing) effectors. This phosphoproteomics data will be instrumental for studies on oomycetes and host-oomycete interactions. The data sets have been deposited to ProteomeXchange (identifier PXD000433).

AB - The oomycete Phytophthora infestans is the causal agent of late blight in potato and tomato. Since the underlying processes that govern pathogenicity and development in P. infestans are largely unknown, we have performed a large-scale phosphoproteomics study of six different P. infestans life stages. We have obtained quantitative data for 2922 phosphopeptides and compared their abundance. Life-stage-specific phosphopeptides include ATP-binding cassette transporters and a kinase that only occurs in appressoria. In an extended data set, we identified 2179 phosphorylation sites and deduced 22 phosphomotifs. Several of the phosphomotifs matched consensus sequences of kinases that occur in P. infestans but not Arabidopsis. In addition, we detected tyrosine phosphopeptides that are potential targets of kinases resembling mammalian tyrosine kinases. Among the phosphorylated proteins are members of the RXLR and Crinkler effector families. The latter are phosphorylated in several life stages and at multiple positions, in sites that are conserved between different members of the Crinkler family. This indicates that proteins in the Crinkler family have functions beyond their putative role as (necrosis-inducing) effectors. This phosphoproteomics data will be instrumental for studies on oomycetes and host-oomycete interactions. The data sets have been deposited to ProteomeXchange (identifier PXD000433).

KW - Amino Acid Motifs

KW - Amino Acid Sequence

KW - Life Cycle Stages

KW - Molecular Sequence Data

KW - Phosphopeptides

KW - Phosphoproteins

KW - Phosphorylation

KW - Phytophthora infestans

KW - Protein-Serine-Threonine Kinases

KW - Proteomics

KW - Tissue Culture Techniques

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1021/pr4009095

DO - 10.1021/pr4009095

M3 - Journal article

VL - 13

SP - 1848

EP - 1859

JO - Journal of Proteome Research

JF - Journal of Proteome Research

SN - 1535-3893

IS - 4

ER -

ID: 53678829